[Fragment reaction catalyzed by E. coli ribosomes]. 1977

V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ

It has been shown that 50S subunits of E. coli MRE-600 ribosomes catalyze the reaction of N-(formyl)-methionyl ester of adenosine 5'-phosphate acting as peptide donor, with Phe-tRNA or CACCA-Phe serving as a peptide acceptor. The reaction is stimulated by cytidine 5'phosphate and inhibited by lincomycin, puromycin and chloramphenicol. The obtained results show that the structure of the donor site of peptidyltransferase is completely assembled on the 50S subunit and 30S subunit is not required for its formation.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008034 Lincomycin An antibiotic produced by Streptomyces lincolnensis var. lincolnensis. It has been used in the treatment of staphylococcal, streptococcal, and Bacteroides fragilis infections. Lincolnensin,Lincomycin, (2S-cis)-Isomer,Epilincomycin,Lincocin,Lincomycin A,Lincomycin Hydrochloride,Lincomycin Monohydrochloride,Lincomycin Monohydrochloride, (2S-cis)-Isomer,Lincomycin Monohydrochloride, (L-threo)-Isomer,Lincomycin Monohydrochloride, Hemihydrate,Lincomycin, (L-threo)-Isomer,Hemihydrate Lincomycin Monohydrochloride
D010458 Peptidyl Transferases Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases. Peptidyl Transferase,Peptidyl Translocase,Peptidyl Translocases,Peptidyltransferase,Transpeptidase,Transpeptidases,Peptidyltransferases,Transferase, Peptidyl,Transferases, Peptidyl,Translocase, Peptidyl,Translocases, Peptidyl
D011691 Puromycin A cinnamamido ADENOSINE found in STREPTOMYCES alboniger. It inhibits protein synthesis by binding to RNA. It is an antineoplastic and antitrypanosomal agent and is used in research as an inhibitor of protein synthesis. CL-13900,P-638,Puromycin Dihydrochloride,Puromycin Hydrochloride,Stylomycin,CL 13900,CL13900,P 638,P638
D002701 Chloramphenicol An antibiotic first isolated from cultures of Streptomyces venequelae in 1947 but now produced synthetically. It has a relatively simple structure and was the first broad-spectrum antibiotic to be discovered. It acts by interfering with bacterial protein synthesis and is mainly bacteriostatic. (From Martindale, The Extra Pharmacopoeia, 29th ed, p106) Cloranfenicol,Kloramfenikol,Levomycetin,Amphenicol,Amphenicols,Chlornitromycin,Chlorocid,Chloromycetin,Detreomycin,Ophthochlor,Syntomycin
D003568 Cytidine Monophosphate Cytidine (dihydrogen phosphate). A cytosine nucleotide containing one phosphate group esterified to the sugar moiety in the 2', 3' or 5' position. CMP,Cytidylic Acid,2'-CMP,3'-CMP,Cytidylic Acids,2' CMP,3' CMP,Acid, Cytidylic,Acids, Cytidylic,Monophosphate, Cytidine
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D012270 Ribosomes Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION. Ribosome
D014176 Protein Biosynthesis The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS. Genetic Translation,Peptide Biosynthesis, Ribosomal,Protein Translation,Translation, Genetic,Protein Biosynthesis, Ribosomal,Protein Synthesis, Ribosomal,Ribosomal Peptide Biosynthesis,mRNA Translation,Biosynthesis, Protein,Biosynthesis, Ribosomal Peptide,Biosynthesis, Ribosomal Protein,Genetic Translations,Ribosomal Protein Biosynthesis,Ribosomal Protein Synthesis,Synthesis, Ribosomal Protein,Translation, Protein,Translation, mRNA,mRNA Translations

Related Publications

V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
August 1969, Biochemical and biophysical research communications,
V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
June 1971, Nature: New biology,
V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
January 1981, Nucleic acids symposium series,
V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
January 1975, Molekuliarnaia biologiia,
V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
November 1977, Biophysical chemistry,
V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
January 1968, Biokhimiia (Moscow, Russia),
V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
May 1976, Biophysical chemistry,
V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
May 1968, Igaku to seibutsugaku. Medicine and biology,
V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
January 1973, Biokhimiia (Moscow, Russia),
V V Kotusov, and M K Kukhanova, and N E Sal'nikova, and L V Nikolaeva, and A A Kraevskiĭ
February 1967, Die Naturwissenschaften,
Copied contents to your clipboard!